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Conserved domains on  [gi|1370506665|ref|XP_024302004|]
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SMC5-SMC6 complex localization factor protein 1 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 5-85 2.53e-47

BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; SLF1, also termed Smc5/6 localization factor 1, or ankyrin repeat domain-containing protein 32 (ANKRD32), or BRCT domain-containing protein 1 (BRCTD1), plays a role in the DNA damage response (DDR) pathway by regulating post replication repair of UV-damaged DNA and genomic stability maintenance. It is a component of the SLF1-SLF2 complex that acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand break (DSB) sites on chromatin during DNA repair in response to stalled replication forks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


:

Pssm-ID: 349381  Cd Length: 81  Bit Score: 162.68  E-value: 2.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665   5 TPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLD 84
Cdd:cd17750     1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLD 80


                  .
gi 1370506665  85 E 85
Cdd:cd17750    81 E 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-898 6.44e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 6.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 796 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 875
Cdd:COG0666   109 AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DG 186

                          90       100
                  ....*....|....*....|...
gi 1370506665 876 VTPLHDALSNGHVEIGKLLLQHG 898
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAG 209
BRCT super family cl00038
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 127-198 2.74e-09

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


The actual alignment was detected with superfamily member cd17728:

Pssm-ID: 469589  Cd Length: 80  Bit Score: 54.58  E-value: 2.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665 127 WKVVLLVRTDKRsDSLIRVLEAGKANVILPKS----SPSGITHVIASNARIKAEKEKDNFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSPpyslKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
 
Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 5-85 2.53e-47

BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; SLF1, also termed Smc5/6 localization factor 1, or ankyrin repeat domain-containing protein 32 (ANKRD32), or BRCT domain-containing protein 1 (BRCTD1), plays a role in the DNA damage response (DDR) pathway by regulating post replication repair of UV-damaged DNA and genomic stability maintenance. It is a component of the SLF1-SLF2 complex that acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand break (DSB) sites on chromatin during DNA repair in response to stalled replication forks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349381  Cd Length: 81  Bit Score: 162.68  E-value: 2.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665   5 TPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLD 84
Cdd:cd17750     1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLD 80


                  .
gi 1370506665  85 E 85
Cdd:cd17750    81 E 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-898 6.44e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 6.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 796 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 875
Cdd:COG0666   109 AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DG 186

                          90       100
                  ....*....|....*....|...
gi 1370506665 876 VTPLHDALSNGHVEIGKLLLQHG 898
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAG 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
811-898 5.03e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 5.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 811 LHRACINNQVEKLILLLSlPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 890
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 1370506665 891 GKLLLQHG 898
Cdd:pfam12796  77 VKLLLEKG 84
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 127-198 2.74e-09

eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the eighth BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349360  Cd Length: 80  Bit Score: 54.58  E-value: 2.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665 127 WKVVLLVRTDKRsDSLIRVLEAGKANVILPKS----SPSGITHVIASNARIKAEKEKDNFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSPpyslKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 784-899 7.59e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 7.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 784 LSCSKENCPSVVKK-----MNFHKTNLKGETALHRA----CINNQVEKLIL--------------LLSLpGIDINVKDNA 840
Cdd:PHA03100  113 AISKKSNSYSIVEYlldngANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVY 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665 841 GWTPLHEACNYGNTVCVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQHGG 899
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 12-88 5.52e-06

Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of regulator of Ty1 transposition protein 107 (RTT107). It is involved in binding phosphorylated histone H2A.


Pssm-ID: 465266  Cd Length: 91  Bit Score: 45.59  E-value: 5.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665  12 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETTY 88
Cdd:pfam16770  13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 808-899 1.66e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 808 ETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEvdLLTQV------DGVTPLHD 881
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHI 95

                          90
                  ....*....|....*...
gi 1370506665 882 ALSNGHVEIGKLLLQHGG 899
Cdd:cd22192    96 AVVNQNLNLVRELIARGA 113
BRCT smart00292
breast cancer carboxy-terminal domain;
6-74 4.87e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 39.67  E-value: 4.87e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370506665    6 PKHIIQMTG-FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWILTKDYII 74
Cdd:smart00292   5 KGKTFYITGsFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 841-869 3.44e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.44e-03
                           10        20
                   ....*....|....*....|....*....
gi 1370506665  841 GWTPLHEACNYGNTVCVQEILQRCPEVDL 869
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
BRCT_SLF1 cd17750
BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; ...
 5-85 2.53e-47

BRCT domain of SMC5-SMC6 complex localization factor protein 1 (SLF1) and similar proteins; SLF1, also termed Smc5/6 localization factor 1, or ankyrin repeat domain-containing protein 32 (ANKRD32), or BRCT domain-containing protein 1 (BRCTD1), plays a role in the DNA damage response (DDR) pathway by regulating post replication repair of UV-damaged DNA and genomic stability maintenance. It is a component of the SLF1-SLF2 complex that acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand break (DSB) sites on chromatin during DNA repair in response to stalled replication forks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349381  Cd Length: 81  Bit Score: 162.68  E-value: 2.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665   5 TPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLD 84
Cdd:cd17750     1 VQKHIIQLTGFKGEEKEALVKLLLKLDCVFIKSEKYENCTHLIAKKPCRSEKFLAACAAGKWILTKDYIINSAKSGRWLD 80


                  .
gi 1370506665  85 E 85
Cdd:cd17750    81 E 81
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 7-80 2.66e-28

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 108.42  E-value: 2.66e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370506665   7 KHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYK-NCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSG 80
Cdd:cd17738     1 KPVFLLSGFSEDEKKELISIIEKLGGKVLDSDEFDpKCTHLICGKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-898 6.44e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 6.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 796 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 875
Cdd:COG0666   109 AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DG 186

                          90       100
                  ....*....|....*....|...
gi 1370506665 876 VTPLHDALSNGHVEIGKLLLQHG 898
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAG 209
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-898 2.83e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 796 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 875
Cdd:COG0666    76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DG 153

                          90       100
                  ....*....|....*....|...
gi 1370506665 876 VTPLHDALSNGHVEIGKLLLQHG 898
Cdd:COG0666   154 NTPLHLAAANGNLEIVKLLLEAG 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
811-898 5.03e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 5.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 811 LHRACINNQVEKLILLLSlPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQrcpEVDLLTQVDGVTPLHDALSNGHVEI 890
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEI 76


                  ....*...
gi 1370506665 891 GKLLLQHG 898
Cdd:pfam12796  77 VKLLLEKG 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-899 4.32e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 4.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 796 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 875
Cdd:COG0666   142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DG 219

                          90       100
                  ....*....|....*....|....
gi 1370506665 876 VTPLHDALSNGHVEIGKLLLQHGG 899
Cdd:COG0666   220 KTALDLAAENGNLEIVKLLLEAGA 243
BRCT_BRC1_like_rpt5 cd17743
fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ...
 12-80 4.26e-12

fifth BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins; Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contain six BRCT domains. This family corresponds to the fifth one.


Pssm-ID: 349374  Cd Length: 70  Bit Score: 62.26  E-value: 4.26e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665  12 MTGFKMEEKEaLVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSG 80
Cdd:cd17743     5 FTGYKLWTEK-EIKKLKKLGISIV--EDPDECTHLVAPKIVRTEKFLCALAYAPVIVTTDWLEACLKAG 70
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 9-76 5.52e-11

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 58.91  E-value: 5.52e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370506665   9 IIQMTGFKMEEKEALVKLLLKLDCTFIKSeKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHS 76
Cdd:cd00027     2 VICFSGLDDEEREELKKLIEALGGKVSES-LSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPEWLLDC 68
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
803-898 8.50e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 8.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 803 TNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDGVTPLHDA 882
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK-DGLTALLLA 259

                          90
                  ....*....|....*.
gi 1370506665 883 LSNGHVEIGKLLLQHG 898
Cdd:COG0666   260 AAAGAALIVKLLLLAL 275
Ank_2 pfam12796
Ankyrin repeats (3 copies);
786-869 5.42e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 5.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 786 CSKENCPSVVKKM-----NFHKTNLKGETALHRACINNQVEKLILLLSlpGIDINVKDNaGWTPLHEACNYGNTVCVQEI 860
Cdd:pfam12796   4 AAKNGNLELVKLLlengaDANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDN-GRTALHYAARSGHLEIVKLL 80


                  ....*....
gi 1370506665 861 LQRCPEVDL 869
Cdd:pfam12796  81 LEKGADINV 89
BRCT_TopBP1_rpt8 cd17728
eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed ...
 127-198 2.74e-09

eighth (C-terminal) BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the eighth BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349360  Cd Length: 80  Bit Score: 54.58  E-value: 2.74e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665 127 WKVVLLVRTDKRsDSLIRVLEAGKANVILPKS----SPSGITHVIASNARIKAEKEKDNFKAPFYP---IQYLGDFLLE 198
Cdd:cd17728     2 WKVLLVVDIAKE-DGFKRLLEAGGAKVIPSSPpyslKLKDATHAFVDLTKDTSVDLISLLAKAGVPclkPEYIAEYLMK 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
845-900 1.45e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.81  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506665 845 LHEACNYGNTVCVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKLLLQHGGV 900
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHADV 55
BRCT_PAXIP1_rpt5 cd17712
fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 13-83 5.64e-07

fifth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fifth BRCT domain.


Pssm-ID: 349344  Cd Length: 75  Bit Score: 47.62  E-value: 5.64e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370506665  13 TGFKMEEKEALVKLLLKLDCTFIKSEKykNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWL 83
Cdd:cd17712     7 TGFDPVQVRKLTKKVTILGGEVVESPQ--ECTHLVAPKVSRTVKFLTAISVCKHIVTPEWLEESFKQGKFL 75
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 784-899 7.59e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 7.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 784 LSCSKENCPSVVKK-----MNFHKTNLKGETALHRA----CINNQVEKLIL--------------LLSLpGIDINVKDNA 840
Cdd:PHA03100  113 AISKKSNSYSIVEYlldngANVNIKNSDGENLLHLYlesnKIDLKILKLLIdkgvdinaknrvnyLLSY-GVPINIKDVY 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665 841 GWTPLHEACNYGNTVCVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQHGG 899
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGP 249
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 8-83 1.81e-06

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 46.43  E-value: 1.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506665   8 HIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWL 83
Cdd:cd17736     1 RTLVMTSVHSEEQELLESVVKKLGGFRVEDSVTEKTTHVVVGSPRRTLNVLLGIARGCWILSPDWVLESLEAGKWL 76
BRCT_MDC1_rpt1 cd17744
first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; ...
 17-83 3.75e-06

first BRCT domain of mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also termed nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S phase and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The family corresponds to the first BRCT domain.


Pssm-ID: 349375 [Multi-domain]  Cd Length: 72  Bit Score: 45.30  E-value: 3.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370506665  17 MEEKEALVKLLLKLDCTFIKSekYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWL 83
Cdd:cd17744     8 VSDKEEGEKIIKKLGGSVVDS--VEDCTHLVTDKVRRTVKFLCALARGIPIVSPDWLEASIKANKFL 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
 803-895 4.91e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 803 TNLKGETALHRA-----CINNQVEKLILllslPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDGVT 877
Cdd:PHA03095  218 TDMLGNTPLHSMatgssCKRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNT 292

                          90
                  ....*....|....*...
gi 1370506665 878 PLHDALSNGHVEIGKLLL 895
Cdd:PHA03095  293 PLSLMVRNNNGRAVRAAL 310
RTT107_BRCT_5 pfam16770
Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of ...
 12-88 5.52e-06

Regulator of Ty1 transposition protein 107 BRCT domain; This is the fifth BRCT domain of regulator of Ty1 transposition protein 107 (RTT107). It is involved in binding phosphorylated histone H2A.


Pssm-ID: 465266  Cd Length: 91  Bit Score: 45.59  E-value: 5.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665  12 MTGFKMEEK--EALVKLLLKLDCTFIksEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETTY 88
Cdd:pfam16770  13 LTGCERWIDkeDLDKKKLRLLGIKIV--QDPSKCNHLIAPKILRTEKFLCALAFAPYILSPDFITDCLKEGKLPDEEDY 89
Ank_5 pfam13857
Ankyrin repeats (many copies);
798-848 7.44e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 7.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370506665 798 MNFHKTNLKGETALHRACINNQVEKLILLLsLPGIDINVKDNAGWTPLHEA 848
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
809-858 1.08e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370506665 809 TALHRACINNQVEkLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQ 858
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 803-868 2.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 2.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506665 803 TNLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVD 868
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
BRCT_nibrin cd17741
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ...
 18-73 2.57e-05

BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group.


Pssm-ID: 349372 [Multi-domain]  Cd Length: 74  Bit Score: 42.97  E-value: 2.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506665  18 EEKEALVKLLLKLDCTFIKsEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYI 73
Cdd:cd17741    13 EEKKKLKQIIAKLGGKVVN-EWTEECTHLVMSKIKVTVKVICALISGKPIVTPEYL 67
Ank_4 pfam13637
Ankyrin repeats (many copies);
841-895 2.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370506665 841 GWTPLHEACNYGNTVCVQEILQRCPEVDLlTQVDGVTPLHDALSNGHVEIGKLLL 895
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 9-80 4.33e-05

second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.


Pssm-ID: 349363 [Multi-domain]  Cd Length: 77  Bit Score: 42.53  E-value: 4.33e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506665   9 IIQMTGFKMEEKEALVKLLLKLDCTFIKSEKyKNCTHLIAERLcKSEKFLAACaagKW----ILTKDYIIHSAKSG 80
Cdd:cd17731     7 VICVTGFDSEERKEIQQLVEQNGGSYSPDLS-KNCTHLIAGSP-SGQKYEFAR---KWnsihIVTPEWLYDSIEAG 77
PHA03095 PHA03095
ankyrin-like protein; Provisional
 784-898 5.36e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 784 LSCSKENCPSVVKKM-----NFHKTNLKGETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHeACNYGNTV--C 856
Cdd:PHA03095   55 LHYSSEKVKDIVRLLleagaDVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFNInpK 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370506665 857 VQEILQRcPEVDL-LTQVDGVTPLHDALSNGHVEIG--KLLLQHG 898
Cdd:PHA03095  134 VIRLLLR-KGADVnALDLYGMTPLAVLLKSRNANVEllRLLIDAG 177
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 802-898 5.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 802 KTNLKGETALHRACiNNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVdGVTPLHD 881
Cdd:PHA02878  163 KDRHKGNTALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC-GNTPLHI 240

                          90
                  ....*....|....*...
gi 1370506665 882 ALSN-GHVEIGKLLLQHG 898
Cdd:PHA02878  241 SVGYcKDYDILKLLLEHG 258
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 808-899 1.66e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 808 ETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEvdLLTQV------DGVTPLHD 881
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyQGETALHI 95

                          90
                  ....*....|....*...
gi 1370506665 882 ALSNGHVEIGKLLLQHGG 899
Cdd:cd22192    96 AVVNQNLNLVRELIARGA 113
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 804-883 1.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 804 NLKGETALHRACINNQVEkLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDGVTPLHDAL 883
Cdd:PHA02874  154 DDNGCYPIHIAIKHNFFD-IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAI 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 825-897 1.84e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370506665 825 LLLSlPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDGVTPLHDALSNGHVEIGKLLLQH 897
Cdd:PTZ00322  100 ILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEENGFREVVQLLSRH 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
796-898 3.12e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 796 KKMNFHKTNLKGETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQvDG 875
Cdd:COG0666     9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GG 87

                          90       100
                  ....*....|....*....|...
gi 1370506665 876 VTPLHDALSNGHVEIGKLLLQHG 898
Cdd:COG0666    88 NTLLHAAARNGDLEIVKLLLEAG 110
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 13-83 3.47e-04

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 39.89  E-value: 3.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370506665  13 TGFKMEEKEALVKLLLKLDCTfIKSEKYKNCTHLIAE----RLCKSE-KFLAACAAGKWILTKDYIIHSAKSGRWL 83
Cdd:cd17734     6 SGLSSEQKKLLEKLAQLLKAK-VVTEFSPEVTHVVVPaderGVCPRTmKYLMGILAGKWIVSFEWVEACLKAKKLV 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
804-838 3.77e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 3.77e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1370506665 804 NLKGETALHRACINNQVEKLILLLSLpGIDINVKD 838
Cdd:pfam12796  58 KDNGRTALHYAARSGHLEIVKLLLEK-GADINVKD 91
BRCT smart00292
breast cancer carboxy-terminal domain;
6-74 4.87e-04

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 39.67  E-value: 4.87e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370506665    6 PKHIIQMTG-FKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERL-CKSEKFLAACAAGKWILTKDYII 74
Cdd:smart00292   5 KGKTFYITGsFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPeGGKLELLKAIALGIPIVKEEWLL 75
Ank_5 pfam13857
Ankyrin repeats (many copies);
826-880 1.73e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370506665 826 LLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRcPEVDLLTQVDGVTPLH 880
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 804-898 1.93e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 804 NLKGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLlTQVDGVTPLHDAL 883
Cdd:PHA02874  121 DAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV-KDNNGESPLHNAA 198

                          90
                  ....*....|....*
gi 1370506665 884 SNGHVEIGKLLLQHG 898
Cdd:PHA02874  199 EYGDYACIKLLIDHG 213
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 13-89 2.03e-03

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 38.48  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665  13 TGFKMEEKEALVKLLLKLDCTFiKSEKYKNCTHLI----AERLC-KSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETT 87
Cdd:cd17735     6 SGLTPEELMLVQKFARKTGSTL-TSQFTEETTHVImktdAELVCeRTLKYFLGIAGRKWVVSYQWITQSIKEGKILPEHD 84


                  ..
gi 1370506665  88 YE 89
Cdd:cd17735    85 FE 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 808-897 2.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 808 ETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLlTQVDGVTPLHDALSNGH 887
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI-PNTDKFSPLHLAVMMGD 147

                          90
                  ....*....|
gi 1370506665 888 VEIGKLLLQH 897
Cdd:PHA02875  148 IKGIELLIDH 157
BRCT_PAXIP1_rpt2 cd17710
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ...
 41-85 2.60e-03

second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain.


Pssm-ID: 349342 [Multi-domain]  Cd Length: 81  Bit Score: 37.60  E-value: 2.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370506665  41 KNCTHLIAERlCKSEKFLAACAAGKW-ILTKDYIIHSAKSGRWLDE 85
Cdd:cd17710    37 KKCTHLVTGK-ASGAKYECALKHEGIkIVTPDWVTDCIKAKTLLDE 81
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 820-898 3.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 3.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370506665 820 VEKLILLLSLPGIDiNVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQHG 898
Cdd:PHA02875   48 SEAIKLLMKHGAIP-DVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG 125
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 841-869 3.44e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.44e-03
                           10        20
                   ....*....|....*....|....*....
gi 1370506665  841 GWTPLHEACNYGNTVCVQEILQRCPEVDL 869
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 801-870 4.45e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 4.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370506665 801 HKTNLKGETALHRA-CINNQV--EKLILLlslpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLL 870
Cdd:PHA03095  251 NARNRYGQTPLHYAaVFNNPRacRRLIAL----GADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 831-897 4.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 4.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370506665 831 GIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTqVDGVTPLHDALSNGHVEIGKLLLQH 897
Cdd:PHA02876  168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA-LDDLSVLECAVDSKNIDTIKAIIDN 233
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 815-898 5.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 815 CINNQVEKLILLlslPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDlLTQVDGVTPLHDALSNGHVEIGKLL 894
Cdd:PHA02874  101 CIEKDMIKTILD---CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLL 176


                  ....
gi 1370506665 895 LQHG 898
Cdd:PHA02874  177 LEKG 180
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 788-898 5.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 788 KENCPSVVKKM-----NFHKTNLKGETALHRACINNQVE----KLILLLSLPGIDINVKDNAGWTPLHEACNY--GNTVC 856
Cdd:PHA03100   44 EARNIDVVKILldngaDINSSTKNNSTPLHYLSNIKYNLtdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSI 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370506665 857 VQEILQRCPEVDLLTqVDGVTPLHDALSNGHV--EIGKLLLQHG 898
Cdd:PHA03100  124 VEYLLDNGANVNIKN-SDGENLLHLYLESNKIdlKILKLLIDKG 166
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 806-898 5.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370506665 806 KGETALHRACINNQVEKLILLLSLpGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDlLTQVDGVTPLHDALSN 885
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD-IEDCCGCTPLIIAMAK 178

                          90
                  ....*....|...
gi 1370506665 886 GHVEIGKLLLQHG 898
Cdd:PHA02875  179 GDIAICKMLLDSG 191
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 806-836 7.64e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.64e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1370506665 806 KGETALHRACINNQVEKLILLLSlPGIDINV 836
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLE-NGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 874-898 8.64e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 8.64e-03
                          10        20
                  ....*....|....*....|....*.
gi 1370506665 874 DGVTPLHDA-LSNGHVEIGKLLLQHG 898
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKG 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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